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Reviewed, UniProtKB/Swiss-Prot P32019 (I5P2_HUMAN)

Last modified February 9, 2010. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Type II inositol-1,4,5-trisphosphate 5-phosphatase
    EC=3.1.3.36
Alternative name(s):
    Phosphoinositide 5-phosphatase
      Short name=5PTase
    75 kDa inositol polyphosphate-5-phosphatase
Gene names
Name: INPP5B
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length993 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Hydrolyzes the calcium-mobilizing second messenger Ins(1,4,5)P3, this is a signal-terminating reaction.

Catalytic activity

1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1-phosphatidyl-1D-myo-inositol 4-phosphate + phosphate.

Tissue specificity

Platelets.

Sequence similarities

Belongs to the inositol-1,4,5-trisphosphate 5-phosphatase type II family.

Contains 1 Rho-GAP domain.

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P32019-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Note: No experimental confirmation available.
Isoform 2 (identifier: P32019-2)

The sequence of this isoform differs from the canonical sequence as follows:
     178-257: Missing.
Isoform 3 (identifier: P32019-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-244: Missing.
Isoform 4 (identifier: P32019-4)

The sequence of this isoform differs from the canonical sequence as follows:
     810-828: TLMPVWTGDDGSQLDSPME → LAYLAAYCFETQLVTKSLI
     829-993: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide1 – 320320
PRO_0000015639
Chain321 – 993673Type II inositol-1,4,5-trisphosphate 5-phosphatase
PRO_0000015640

Regions

Domain821 – 993173Rho-GAP

Natural variations

Alternative sequence1 – 244244Missing in isoform 3.
VSP_012821
Alternative sequence178 – 25780Missing in isoform 2.
VSP_012820
Alternative sequence810 – 82819TLMPV…DSPME → LAYLAAYCFETQLVTKSLI in isoform 4.
VSP_013902
Alternative sequence829 – 993165Missing in isoform 4.
VSP_013903
Natural variant461G → S: dbSNP rs56993041.
VAR_061270
Natural variant7451M → T: dbSNP rs11488569. Ref.1 Ref.3 Ref.5
VAR_028002

Experimental info

Sequence conflict587 – 60620GSDDW…WCDRI → RALTTGIPVRSAVLLPGVIG F AA sequence Ref.5
Sequence conflict9111G → P AA sequence Ref.5

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified December 15, 2009. Version 4.
Checksum: ABD3581CC6CD29D6

FASTA993112,852
        10         20         30         40         50         60 
MDQSVAIQET LAEGEYCVIA VQGVLCEGDS RQSRLLGLVR YRLEHGGQEH ALFLYTHRRM 

        70         80         90        100        110        120 
AITGDDVSLD QIVPVSRDFT LEEVSPDGEL YILGSDVTVQ LDTAELSLVF QLPFGSQTRM 

       130        140        150        160        170        180 
FLHEVARACP GFDSATRDPE FLWLSRYRCA ELELEMPTPR GCNSALVTWP GYATIGGGRY 

       190        200        210        220        230        240 
PSRKKRWGLE EARPQGAGSV LFWGGAMEKT GFRLMERAHG GGFVWGRSAR DGRRDEELEE 

       250        260        270        280        290        300 
AGREMSAAAG SRERNTAGGS NFDGLRPNGK GVPMDQSSRG QDKPESLQPR QNKSKSEITD 

       310        320        330        340        350        360 
MVRSSTITVS DKAHILSMQK FGLRDTIVKS HLLQKEEDYT YIQNFRFFAG TYNVNGQSPK 

       370        380        390        400        410        420 
ECLRLWLSNG IQAPDVYCVG FQELDLSKEA FFFHDTPKEE EWFKAVSEGL HPDAKYAKVK 

       430        440        450        460        470        480 
LIRLVGIMLL LYVKQEHAAY ISEVEAETVG TGIMGRMGNK GGVAIRFQFH NTSICVVNSH 

       490        500        510        520        530        540 
LAAHIEEYER RNQDYKDICS RMQFCQPDPS LPPLTISNHD VILWLGDLNY RIEELDVEKV 

       550        560        570        580        590        600 
KKLIEEKDFQ MLYAYDQLKI QVAAKTVFEG FTEGELTFQP TYKYDTGSDD WDTSEKCRAP 

       610        620        630        640        650        660 
AWCDRILWKG KNITQLSYQS HMALKTSDHK PVSSVFDIGV RVVNDELYRK TLEEIVRSLD 

       670        680        690        700        710        720 
KMENANIPSV SLSKREFCFQ NVKYMQLKVE SFTIHNGQVP CHFEFINKPD EESYCKQWLN 

       730        740        750        760        770        780 
ANPSRGFLLP DSDVEIDLEL FVNKMTATKL NSGEDKIEDI LVLHLDRGKD YFLSVSGNYL 

       790        800        810        820        830        840 
PSCFGSPIHT LCYMREPILD LPLETISELT LMPVWTGDDG SQLDSPMEIP KELWMMVDYL 

       850        860        870        880        890        900 
YRNAVQQEDL FQQPGLRSEF EHIRDCLDTG MIDNLSASNH SVAEALLLFL ESLPEPVICY 

       910        920        930        940        950        960 
STYHNCLECS GNYTASKQVI STLPIFHKNV FHYLMAFLRE LLKNSAKNHL DENILASIFG 

       970        980        990 
SLLLRNPAGH QKLDMTEKKK AQEFIHQFLC NPL 

« Hide

Isoform 2.

Checksum: 4882C26F6E4DC9C6
Show »

FASTA913103,987
Isoform 3.

Checksum: 50921FAACF7E1E39
Show »

FASTA74985,620
Isoform 4.

Checksum: 9CD5C12DCF509A50
Show »

FASTA82893,924

References

« Hide 'large scale' references
[1]"Properties of type II inositol polyphosphate 5-phosphatase."
Jefferson A.B., Majerus P.W.
J. Biol. Chem. 270:9370-9377(1995) [PubMed: 7721860] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT THR-745.
[2]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed: 16710414] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORMS 1; 2 AND 3).
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), VARIANT THR-745.
Tissue: Lymph.
[4]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-178.
Tissue: Stomach.
[5]"Cloning and expression of human 75-kDa inositol polyphosphate-5-phosphatase."
Ross T.S., Jefferson A.B., Mitchell C.A., Majerus P.W.
J. Biol. Chem. 266:20283-20289(1991) [PubMed: 1718960] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 284-954, PROTEIN SEQUENCE OF 321-339, VARIANT THR-745.
Tissue: Placenta.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M74161 mRNA. Translation: AAA79207.1. Different initiation.
AL603790, AL929472 Genomic DNA. Translation: CAH69926.1.
AL603790, AL929472 Genomic DNA. Translation: CAH69928.1.
AL603790, AL929472 Genomic DNA. Translation: CAH69929.1.
AL929472, AL603790 Genomic DNA. Translation: CAH70076.1.
AL929472, AL603790 Genomic DNA. Translation: CAH70079.1.
AL929472, AL603790 Genomic DNA. Translation: CAH70080.1.
BC042529 mRNA. Translation: AAH42529.2.
BC058932 mRNA. Translation: AAH58932.1.
AL833055 mRNA. Translation: CAH56301.1.
IPIIPI00244111.
IPI00478376.
IPI00553072.
IPI00604769.
RefSeqNP_005531.2.
UniGeneHs.449942

3D structure databases

SMRP32019. Positions 325-664, 673-991.
ModBaseSearch...

Protein-protein interaction databases

STRINGP32019.

PTM databases

PhosphoSiteP32019.

Genome annotation databases

EnsemblENST00000373023; ENSP00000362114; ENSG00000204084; Homo sapiens. [Genome view]
ENST00000373026; ENSP00000362117; ENSG00000204084; Homo sapiens. [Genome view]
GeneID3633.
KEGGhsa:3633.
UCSCuc001ccf.1. human.
uc001ccg.1. human.
uc009vvk.1. human.

Organism-specific databases

CTD3633.
GeneCardsGC01M038162.
H-InvDBHIX0000445.
HGNCHGNC:6077. INPP5B.
MIM147264. gene.
PharmGKBPA29885.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG04448.
HOVERGENP32019.
InParanoidP32019.

Enzyme and pathway databases

BioCycMetaCyc:ENSG00000134678-MONOMER.
BRENDA3.1.3.36. 247.
ReactomeREACT_11044. Signaling by Rho GTPases.

Gene expression databases

ArrayExpressP32019.
BgeeP32019.
CleanExHS_INPP5B.
GenevestigatorP32019.
GermOnlineENSG00000204084. Homo sapiens.

Family and domain databases

InterProIPR005135. Endo/exonuclease/phosphatase.
IPR000300. IPPc.
IPR008936. Rho_GTPase_activation_prot.
IPR000198. RhoGAP.
[Graphical view]
Gene3DG3DSA:1.10.555.10. RhoGAP. 1 hit.
PfamPF03372. Exo_endo_phos. 1 hit.
PF00620. RhoGAP. 1 hit.
[Graphical view]
SMARTSM00128. IPPc. 1 hit.
SM00324. RhoGAP. 1 hit.
[Graphical view]
PROSITEPS50238. RHOGAP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio14219.
SOURCESearch...

Entry information

Entry nameI5P2_HUMAN
AccessionPrimary (citable) accession number: P32019
Secondary accession number(s): Q5VSG9 expand/collapse secondary AC list , Q5VSH0, Q5VSH1, Q658Q5, Q6P6D4, Q6PD53, Q86YE1
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: December 15, 2009
Last modified: February 9, 2010
This is version 92 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents